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In recent years, the demand for foods without animal proteins has increased, both for health and ethical reasons. Replacing animal protein in foods can result in unappealing textures, hindering consumer acceptance. In this context, interfacial properties also play a crucial role in food systems like foam or emulsions. Therefore, the interfacial rheological behavior at the air–water interface of pea protein isolate (PPI) has been investigated to understand how affects food foam production. The PPI has been studied without modification and also through enzymatic treatment with transglutaminase (TG) to understand the interfacial properties of the modified proteins. Data obtained by static measurements have shown a surface activity of PPI comparable with other vegetable proteins, while the treatment with TG does not significantly alter the surface tension value and the interfacial adsorption rate. Differences have been found in the rearrangement rate, which decreases with TG, suggesting a possible crosslinking of the pea proteins. The PPI modified with TG, studied in dynamic conditions both in dilation and shear kinematics, are less elastic than PPI that is untreated but with a higher consistency, which may lead to poor foam stability. The lower complex interfacial modulus obtained under shear conditions also suggests a low long-time stability. [ABSTRACT FROM AUTHOR]

Colloidal food products, such as emulsions, foams, gels, and dispersions, are complex systems that need the presence of stabilizing agents to enable their formation and provide stability. Proteins are often used for food foams and emulsions because of their ability to lower interfacial tension and make viscoelastic interfaces. Generally, to improve the resistance against rupture, polysaccharides are used in association with the proteins. Pectin is a complex polysaccharide that can help to stabilize foams or emulsions. This work aims at studying the mechanical resistance of the interface formed by mixtures of β-casein and pectin at high and low methoxylation degrees at the air/water interface using dilatational and shear kinematics. Frequency sweep tests, in the linear region, were performed in shear at different aging times and in dilatational mode, and the rheological data were analyzed. The transient data of the surface tension were analyzed by kinetic models to obtain the characteristic rates of the interfacial phenomena. The kinetic mechanisms of the protein/pectin mixed systems are controlled by protein and show a weak gel behavior for short aging times. The interfaces obtained with both pectins in a mixture with β-casein evolved with time, gelling and showing a solid-like behavior at concentrations of 1 and 10 g/L and after 3.5 h of aging time. The interfacial shear trend obtained suggests a good stabilizing effect of the pectins from citrus with long aging times. [ABSTRACT FROM AUTHOR]